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Title: FK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53T
Authors: GĂ©rard, Melanie
Debyser, Zeger
Desender, Linda
Baert, Johan
Brandt, Inger
Baekelandt, Veerle ×
Engelborghs, Yves #
Issue Date: Jul-2008
Publisher: Raven Press
Series Title: Journal of Neurochemistry vol:106 issue:1 pages:121-133
Abstract: Aggregation of alpha-synuclein (alpha-SYN) plays a key role in Parkinson's disease. We have previously shown that aggregation of alpha-SYN in vitro is accelerated by addition of FK506 binding proteins (FKBP) and that this effect can be counteracted by FK506, a specific inhibitor of these enzymes. In this paper, we investigated in detail the effect of FKBP12 on early aggregation and on fibril formation of wild-type, A53T and A30P alpha-SYN. FKBP12 has a much smaller effect on the fibril formation of these two clinical mutants alpha-SYN. Using an inactive enzyme, we were able to discriminate between catalytic and non-catalytic effects that differentially influence the two processes. A model explaining non-linear concentration dependencies is proposed.
URI: 
ISSN: 0022-3042
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Virology and Gene Therapy
Interdisciplinary Research Facility Life Sciences, Campus Kulak Kortrijk
Research Group for Neurobiology and Gene Therapy
Biochemistry, Molecular and Structural Biology Section
Biochemistry, Kulak (-)
× corresponding author
# (joint) last author

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